Overview

Hydrophobic peptides are difficult to prepare and handle, making their study or use in biological research difficult. For example, β-amyloids, which are highly hydrophobic peptides, are prone to natural self-assembly. These peptides aggregate and deposit on organs, forming debilitating plaques that are involved in the progression of many neurodegenerative diseases such as Alzheimer's and Parkinson's, as well as other diseases such as diabetes and Huntington's. β-amyloids are targets for developing effective therapies to treat these diseases, but these studies are often hindered by uncontrollable aggregative nature of β-amyloids.

Key Features

Click Peptide Synthesis allows
control over

  • Physicochemical peptide properties (e.g., water-solubility, self-assembly, aggregation, or folding)
  • Biologic activities (e.g., ligand-receptor binding affinity, orenzyme-substrate binding affinity)

Control over Click Peptide to
native peptide conversion

  • Click peptide converts to native peptide easily at pH7.4 or above
  • Conversion is a one-way, quick process
  • No by-product formation during conversion, suitable for biological experiments

Key Advantages

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Increases peptide solubility

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Slows peptide aggregation

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Novel system useful for investigating the dynamic biological functions of β-amyloids in neurodegenerative diseases and other diseases exhibiting amyloidosis

Service Details

Quotations and Ordering

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